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Contact data |
Full Professor
Department of Biotechnology and Molecular Sciences
Via J.H. Dunant 3 - 21100 Varese - Italy
Tel: +39 (0)332 421320
Fax: +39 (0)332 421300
E-mail: antonio.peres@uninsubria.it
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Biography |
Born in 1949 in Vercelli
(Italy). In 1972, earned degree in Physics at the University of
Turin, with a thesis on the biophysical theories of cell membrane
permeation. In 1973/74, Fulbright Fellow at the Department of Physiology,
University of Rochester, N.Y., USA (Prof. M.F. Schneider) working
on the development of optical methods for the measurement of intracellular
calcium in skeletal muscle fibres. In 1974/75 and 1977-1983, Research
Fellow at the Department of General Physiology and Biochemistry
of the University of Milan (Prof. A. Ferroni), working on the electrophysiological
properties of skeletal muscle fibres and of Xenopus laevis oocytes.
In 1976/77, granted an EMBO Fellowship to gain experience on voltage-clamp
techniques on skeletal muscle fibres at the Physiological Laboratory,
University of Cambridge, U.K. (Prof. R.H. Adrian). During this period
the problem of excitation-contraction coupling is investigated,
through experiments on intramembrane charge movements in skeletal
muscle fibres. In 1983 became Associate Professor of Cell Physiology
at the Department of General Physiology and Biochemistry of the
University of Milan. In these years the research interest is devoted
to studies on calcium regulation in mammalian oocytes and cell lines,
channel modulation and calcium signaling induced by mitogens and
growth factors.
In 1994 becomes Full Professor of General Physiology at the Department
of Physiology of the University of Florence.
From 1995 to present is Full Professor of General Physiology at
the Department of Structural and Functional Biology of the University
of Insubria, where the main research focus is on the study of the
mechanisms and modulation of membrane channels and neurotransmitter
transporters. In 2003 spent a research period at the Department
of Pharmacology, University of Cambridge, UK (Prof. P.A. McNaughton).
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Qualifications and awards |
Member of the Italian Physiological
Society, of the American Physiological Society, of the Biophysical
Society, and of the Society of General Physiologists. |
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Research interests |
The present research activity
is focused on the molecular physiology and biophysics of membrane
transport proteins. In particular, in the last years the study of
neurotransmitter cotransporters has received the major attention.
The physiological roles of these molecules include recovery of the
neurotransmitter released at synapses for its recycling and modulation
of synaptic activity. They are involved in various neurological disorders
and may be targets of therapeutical drugs. Many of these proteins
have been cloned and may be overexpressed in heterologous systems,
where they may be studied in detail using various experimental techniques.
In the Laboratory of Cellular and Molecular Physiology (LFCM) at the
DBSF in Varese, the physiological and biophysical properties of the
neuronal GABA transporter rGAT1 (and of other cotransporters as well)
are studied using electrophysiology (voltage-clamp, patch-clamp),
optical methods (confocal fluorescence microscopy and fluoresence
resonance energy transfer), and molecular biology (site-directed mutagenesis,
chimeric constructs and concatemers). The results of the recent years
of activity concern the description of parts of the transport cycle,
structure-function studies, identification of domains involved in
ion and substrate interaction, and modelling of the transport mechanism.
Further information may be found in the LFCM pages (http://fisio.dipbsf.uninsubria.it/lfcm/). |
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Teaching experience and appointments |
The teaching activity
began in 1976 and continued without interruption, first in Cell Physiology
courses at the University of Milan, for the Degree in Biology, and
subsequently in General Physiology courses at the University of Florence
(for the degree in Pharmacy), and the University of Insubria, for
the Degrees in Biology, Biotechnology and Natural Sciences. Additional
courses in Biophysics and Cell Physiology were also held. Lectures
were given in PhD courses as well.
Director of the Department of Structural and Functional Biology
for the years 2000- 2002 and 2004-2007.
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Representative publications |
1. Soragna,A. Bossi,E., Giovannardi,S., Pisani,R., and Peres,A. Functionally
independent subunits in the oligomeric structure of the GABA cotransporter
rGAT1. CMLS. In press. 2005.
2. Soragna,A. Bossi,E., Giovannardi,S., Pisani,R., and Peres,A. Relations
between substrate affinities and charge equilibration rates in the
GABA cotransporter rGAT1. J.Physiol. 562:333-345. 2005.
3. Soragna,A. Mari,S. Peres,A., Pisani,R., Castagna,M., Sacchi,V.F.
and Bossi,E. Structural domains involved in substrate selectivity
in two neutral amino acid transporters. Am. J. Physiol. Cell Physiol.
287:C754-761. 2004.
4. Peres,A. Giovannardi,S. Bossi,E. and Fesce,R. Electrophysiological
insights on the mechanism of ion-coupled cotransporters. NIPS. 19:80-84.
2004.
5. Mari,S.A., Soragna,A., Castagna,M., Bossi, E., Peres,A. and V.F.
Sacchi. Aspartate 338 contributes to the cationic specificity and
to the driver-amino acid coupling in the insect cotransporter KAAT1.
CMLS. 61:243-256. 2004.
6. Sacchi, V.F., Castagna, M., Mari, S.A., Bossi, E. and A. Peres.
Glutamate 59 is critical for transport function of the amino acid
cotransporter KAAT1. Am. J. Physiol. Cell Physiol. 285:C623-632. 2003.
7. Giovannardi, S., Fesce, R., Bossi, E., Binda, F. and A. Peres.
Cl- affects the function of the gaba cotransporter rGAT1 but preserves
the mutual relation between transient and transport currents. CMLS.
60:550-556. 2003.
8. Fesce, R., Giovannardi, S., Binda, F., Bossi, E. and A. Peres.
The relation between charge movement and transport-associated currents
in the GABA cotransporter rGAT1. J. Physiol. 545:739-750. 2002.
9. Bossi, E., Giovannardi, S., Binda, F., Forlani, G. and A. Peres.
Role of anion-cation interactions on the pre-steady-state currents
of the rat Na+ -Cl- dependent GABA cotransporter rGAT1. J. Physiol.
541:343-350. 2002.
10. Giovannardi, S,. G. Forlani, M. Balestrini, E. Bossi,R. Tonini,
E. Sturani, A. Peres and R. Zippel. Modulation of the inward rectifier
potassium channel IRK1 by the Ras signaling pathway. J.Biol. Chem.
277:12158-12163. 2002.
11. Binda, F,. E. Bossi, S. Giovannardi, G. Forlani, and A. Peres.
Temperature effects on the presteady-state and transport-associated
currents of GABA cotransporter rGAT1. FEBS Letters, 512:303-307. 2002.
12. Forlani, G.,E. Bossi, R. Ghirardelli, S. Giovannardi, F. Binda,
L. Bonadiman, L. Ielmini and A. Peres. K448E mutation in the external
loop 5 of rGAT1 transporter induces pH sensitivity and altered substrates
interactions. J. Physiol. 36:47-494. 2001.
13. Forlani, G., E. Bossi, C. Perego, S. Giovannardi and A. Peres.
Three kinds of currents in the canine Betaine/GABA transporter BGT-1
expressed in Xenopus laevis oocytes. Biochim.Biophys.Acta Mol. Cell
Res. 1538:172-180. 2001.
14. Peres,A and E. Bossi. Effects of pH on the uncoupled, coupled
and presteady-state currents at the amino acid cotransporter KAAT1.
J. Physiol. 525:83-89. 2000.
15. Vincenti, S., M. Castagna, A. Peres and V.F. Sacchi. Substrate
selectivity and pH dependence of KAAT1 expressed in Xenopus laevis
oocytes. J. Membr. Biol. 174:213:224. 2000.
16. Bossi, E., S. Vincenti, V. F. Sacchi and A. Peres. Simultaneous
measurements of ionic currents and leucine uptake at the amino acid
cotransporter KAAT1 expressed in Xenopus laevis oocytes. Biochim.Biophys.Acta
Mol. Cell Res. 1495:34-39. 2000.
17. Bossi, E., V. F. Sacchi and A. Peres. Ionic selectivity of the
coupled and uncoupled currents carried by the amino acid transporter
KAAT1. Pfluegers Arch., 438:788-796. 1999.
18. Bossi, E., E. Centinaio, M. Castagna, S. Giovannardi, S. Vincenti,
V. F.Sacchi and A. Peres. Ion binding and permeation through the lepidopteran
amino acid transporter KAAT1 expressed in Xenopus oocytes. J. Physiol,
51:729-742. 1999.
19. Blumenstein, Y., T. Ivanina, E. Shistik, E. Bossi, A. Peres, and
N. Dascal. Regulation of cardiac L-type Ca2+ channel by coexpression
of Gas in Xenopus oocytes. FEBS Lett. 444:78-84. 1999.
20. Giovannrdi,S., L. Landò,and A. Peres. Flash photolysis
of caged compounds: casting light on physiological processes. NIPS,
13:251-255.1998.
21. Bossi,E., E. Centinaio, A. Moriondo, and A. Peres. Ca2+-dependence
of the depolarization-inducible Na+ current of Xenopus oocytes. J.cell.Physiol.174:154-159,
1998.
22. Centinaio,E., E. Bossi, and A. Peres. Properties of the Ca2+-activated
Cl- current of Xenopus oocytes. Cell.Mol.Life Sci. 53:604-610, 1997.
23. Peres,A. and S. Giovannardi. Characteristics of the signal transduction
system activated by ATP receptors in the hepatoma cell line N1S1-67.
Biochim.Biophys.Acta 1265:33-39, 1995.
24. Giovannardi,S., P. Cesare, and A. Peres. Rapid synchrony of nuclear
and cytosolic Ca2+ signals activated by muscarinic stimulation in
the human tumour line TE671/RD. Cell Calcium 16:491-499, 1994.
25. Lazrak, A. Peres, S. Giovannardi, and C. Peracchia. Ca-mediated
and independent effects of arachidonic aci ongap junctions and Ca-independent
effects of oleic acid and halothane. Biophys.J. 67:1052-1059, 1994.
26. Giovannardi,S., C. Racca, L. Bertollini, E. Sturani, and A. Peres.
P2Y-purinoceptors in normal NIH 3T3 and in NH 3T3 overexpressing c-ras.
Exp.Cell Res. 202:398-404, 1992.
27. Lovisolo,D., G. Bonelli, F. M. Baccino, A. Peres, F. Alonzo, and
L. Munaron. Two currents activated by epidermal growth factor in EGFR-
T17 fibroblasts. Biochim.Biophys.Acta Bio-Membr. 1104:73-82, 1992.
28. Peres, A., L. Bertollini, and C. Racca. Characterization of Ca2+
transients induced by intracellular photorelease of InsP3 in mouse
ovarian oocytes. Cell Calcium 12:457-465, 1991.
29. Brambilla,R., R. Zippel, E. Sturani, L. Morello, A. Peres, and
L. Alberghina. Characterization of the tyrosine phosphorylation of
calpactin I by platelet derived growth factor. Biochem.J. 278:447-452,
1991.
30. Peres, A., L. Bertollini, S. Camagni, and E. Wanke. [Ca2+]i recordings
and the inactivation of the high-voltage activated Ca2+ currents in
the adult rat sensory neuron. Cell Calcium 12:599-608, 1991.
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